Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human GNLY protein.
Granulysin (GNLY) was originally identified as a late activation marker in T cells, and it is expressed by killer lymphocytes in most mammals, but not rodents. GNLY is largely confined to cytotoxic granules but can be secreted by killer cells, especially those expressing high levels of GNLY, such as decidual natural killer cells (1-3). GNLY is produced as a 15 kDa protein and is processed into a 9 kDa active pore-forming fragment by proteolytic removal of peptides from both the N- and C-termini. Moreover, the 15 kDa form was reported to function as an immune alarmin, causing the maturation and migration of antigen-presenting cells and other cells of the immune system (4-7). Unlike perforin, a cholesterol-dependent pore-forming protein that preferentially permeabilizes mammalian membranes, GNLY is inhibited by cholesterol and forms pores much more efficiently in microbial than mammalian membranes, and it plays an important role against bacteria, fungi, and parasite infections (8,9).
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